AMPN_FELCA
ID AMPN_FELCA Reviewed; 967 AA.
AC P79171; O97783;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Aminopeptidase N {ECO:0000305};
DE Short=AP-N;
DE Short=fAPN;
DE EC=3.4.11.2 {ECO:0000250|UniProtKB:P15144};
DE AltName: Full=Alanyl aminopeptidase;
DE AltName: Full=Aminopeptidase M;
DE Short=AP-M;
DE AltName: Full=Microsomal aminopeptidase;
DE AltName: CD_antigen=CD13;
GN Name=ANPEP; Synonyms=APN;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FCOV SPIKE GLYCOPROTEIN
RP (MICROBIAL INFECTION), CHARACTERIZATION OF CORONAVIRUS RECEPTOR FUNCTION
RP (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=8970993; DOI=10.1128/jvi.70.12.8669-8674.1996;
RA Tresnan D.B., Levis R., Holmes K.V.;
RT "Feline aminopeptidase N serves as a receptor for feline, canine, porcine,
RT and human coronaviruses in serogroup I.";
RL J. Virol. 70:8669-8674(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS
RP FOR FIPV INFECTION (MICROBIAL INFECTION), AND TOPOLOGY.
RX PubMed=9782265; DOI=10.1007/978-1-4615-5331-1_8;
RA Kolb A.F., Hegyi A., Maile J., Heister A., Hagemann M., Siddell S.G.;
RT "Molecular analysis of the coronavirus-receptor function of aminopeptidase
RT N.";
RL Adv. Exp. Med. Biol. 440:61-67(1998).
RN [3]
RP IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR FIPV; TGEV AND HCV-229E
RP INFECTION (MICROBIAL INFECTION), AND TOPOLOGY.
RX PubMed=9634079; DOI=10.1099/0022-1317-79-6-1387;
RA Hegyi A., Kolb A.F.;
RT "Characterization of determinants involved in the feline infectious
RT peritonitis virus receptor function of feline aminopeptidase N.";
RL J. Gen. Virol. 79:1387-1391(1998).
RN [4]
RP CHARACTERIZATION OF IBV RECEPTOR FUNCTION (MICROBIAL INFECTION), AND
RP SUBCELLULAR LOCATION.
RX PubMed=12417943; DOI=10.1007/s00705-002-0888-1;
RA Miguel B., Pharr G.T., Wang C.;
RT "The role of feline aminopeptidase N as a receptor for infectious
RT bronchitis virus.";
RL Arch. Virol. 147:2047-2056(2002).
CC -!- FUNCTION: Broad specificity aminopeptidase which plays a role in the
CC final digestion of peptides generated from hydrolysis of proteins by
CC gastric and pancreatic proteases. Also involved in the processing of
CC various peptides including peptide hormones, such as angiotensin III
CC and IV, neuropeptides, and chemokines. May also be involved the
CC cleavage of peptides bound to major histocompatibility complex class II
CC molecules of antigen presenting cells. May have a role in angiogenesis
CC and promote cholesterol crystallization. May have a role in amino acid
CC transport by acting as binding partner of amino acid transporter
CC SLC6A19 and regulating its activity (By similarity).
CC {ECO:0000250|UniProtKB:P15144, ECO:0000250|UniProtKB:P97449}.
CC -!- FUNCTION: (Microbial infection) In case of feline coronavirus (FCoV)
CC infection, serves as a receptor for FCoV spike glycoprotein. It is as
CC well a receptor for other serogroup I coronaviruses, like canine
CC coronavirus (CCoV), porcine transmissible gastroenteritis virus (TGEV),
CC and human coronavirus 229E (HCoV-229E). Also serves as a receptor for
CC infectious bronchitis virus (IBV, Arkansas 99 serotype) in serogroup
CC III. {ECO:0000269|PubMed:12417943, ECO:0000269|PubMed:8970993,
CC ECO:0000269|PubMed:9634079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000250|UniProtKB:P15144};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15144};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15144};
CC -!- SUBUNIT: Homodimer. Interacts with SLC6A19 (By similarity).
CC {ECO:0000250|UniProtKB:P15144, ECO:0000250|UniProtKB:P97449}.
CC -!- SUBUNIT: (Microbial infection) Interacts with FCoV, CCoV, TGEV and
CC HCoV-229E spike glycoprotein. {ECO:0000269|PubMed:8970993,
CC ECO:0000269|PubMed:9634079}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12417943,
CC ECO:0000269|PubMed:8970993}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:9634079, ECO:0000269|PubMed:9782265}. Note=Also
CC found as a soluble form. {ECO:0000250|UniProtKB:P15144}.
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P15144}.
CC -!- PTM: May undergo proteolysis and give rise to a soluble form.
CC {ECO:0000250|UniProtKB:P15144}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; U58920; AAC48686.1; -; mRNA.
DR EMBL; U96104; AAD09272.1; -; mRNA.
DR RefSeq; NP_001009252.2; NM_001009252.2.
DR AlphaFoldDB; P79171; -.
DR SMR; P79171; -.
DR STRING; 9685.ENSFCAP00000008319; -.
DR MEROPS; M01.001; -.
DR GeneID; 493785; -.
DR KEGG; fca:493785; -.
DR CTD; 290; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; P79171; -.
DR OrthoDB; 110058at2759; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Angiogenesis; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Hydrolase;
KW Membrane; Metal-binding; Metalloprotease; Protease; Receptor;
KW Reference proteome; Signal-anchor; Sulfation; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..967
FT /note="Aminopeptidase N"
FT /id="PRO_0000095080"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9782265"
FT TRANSMEM 9..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..967
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:9634079,
FT ECO:0000269|PubMed:9782265"
FT REGION 33..66
FT /note="Cytosolic Ser/Thr-rich junction"
FT REGION 41..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..967
FT /note="Metalloprotease"
FT REGION 670..840
FT /note="Interaction with FCoV and TGEV spike glycoprotein"
FT /evidence="ECO:0000269|PubMed:9634079,
FT ECO:0000269|PubMed:9782265"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 351..355
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 476
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT MOD_RES 175
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 418
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 762..769
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT DISULFID 799..835
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT CONFLICT 105
FT /note="N -> S (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="H -> Q (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="N -> K (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="E -> D (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="I -> T (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="Missing (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="N -> K (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="S -> N (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="L -> V (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="L -> S (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 735..737
FT /note="ERV -> RKS (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="T -> A (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="L -> F (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 949
FT /note="L -> I (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="S -> SK (in Ref. 2; AAD09272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 967 AA; 109424 MW; 119BDAA34F5B5E89 CRC64;
MAKGFYISKP VGILAILLGV AAVCTIIALS VVYSQEKNRS TESSTAASTA APTGPTTTVA
TTLDQSKPWN VYRLPKTLIP DSYNVTLRPY LTPNNKGLYV FTGTNIVRFT CKESTNIVII
HSKRLNYTSH QGHMVALSGV GGFHPQPVIV RTELVELTEY LVVHLQEPLV AGRQYEMNSE
FQGELADDLA GFYRSEYMEN GVKKVLATTH MQATEARKSF PCFDEPAMKA TFNITIIHPN
NLVALSNMLP RGPSVPFGED PTWKVTEFET TPIMSTYLLA YIVSEFSYVE TRAPSGVLIR
IWARPSAINQ GHGDYALKVT GPILDFFSQH YDTPYPLNKS DQIALPDFNA GAMENWGLVT
YRESALLYDR QSSSSGNQER VVTVIAHELA HQWFGNLVTL EWWNDLWLNE GFASYVEYLG
ADFAEPTWNL KDLMVLNDVY RVMAVDALAS SHPLSTPASE INTPAQISEV FDSISYSKGA
SVLRMLSNFL TEDLFKMGIA SYLHTYKYGN TIYLNLWEHL QQVVDKQPTI KLPDTVSAIM
DRWILQMGFP VITVDTQTGT ISQQHFLLDP QSVVTRPSQF NYLWIVPISS VRSGSPQAHY
WLPGVEKAQN DLFKTTANDW VLLNLNVTGY YLVNYDNENW KKIQTQLQTD LSVIPVINRA
QVIHDAFNLA SAQKVPVTLA LNNTLFLIQE TEYMPWQAAL SSLSYFKLMF DRSEVYGPMK
RYLKKQVTPL FNHFERVTKN WTDHPQTLMD QYSEINAVST ACSYGVPECE KLAATLFAQW
KKNPQNNPIH PNLRSTVYCN AIAQGGEEEW NFVWEQFLKA ELVNEADKLR GALACSNQVW
ILNRFLSYTL DPNLIRKQDV TSTLSSISSN VVGQTLVWDF VQSNWKKLFQ DYGTGSFSFS
NLIQAVTRRF STEFELQQLE QFKKNNMDTG FGSATRALEQ ALEKTKANLK WVKENKDVVL
RWFTENS
